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Protein

Endo-alpha-N-acetylgalactosaminidase

Gene

spr0328

Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Is involved in the breakdown of mucin-type O-linked glycans. Specifically removes the T-antigen disaccharide (Gal-beta-1,3-GalNAc-alpha) from extracellular host glycoproteins. Is representative of a broadly important class of virulence factors.3 Publications

Catalytic activityi

3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosaminyl-L-serine-[protein] + H2O = 3-O-beta-D-galactosyl-N-acetyl-alpha-D-galactosamine + L-serine-[protein].1 Publication

Kineticsi

  1. KM=34 µM for Gal-beta-1,3-GalNAc-alpha-2,4-dinitrophenyl1 Publication

    pH dependencei

    Optimum pH is 7.6.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi577Calcium 11 Publication1
    Metal bindingi579Calcium 11 Publication1
    Metal bindingi581Calcium 11 Publication1
    Metal bindingi583Calcium 1; via carbonyl oxygen1 Publication1
    Metal bindingi588Calcium 11 Publication1
    Binding sitei658SubstrateCurated1
    Active sitei764Nucleophile1 Publication1
    Active sitei796Proton donor/Proton acceptor1 Publication1
    Metal bindingi1233Calcium 2; via carbonyl oxygen1 Publication1
    Metal bindingi1235Calcium 21 Publication1
    Metal bindingi1281Calcium 2; via carbonyl oxygen1 Publication1
    Metal bindingi1284Calcium 2; via carbonyl oxygen1 Publication1
    Metal bindingi1411Calcium 21 Publication1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciSPNE171101:GJC8-318-MONOMER.
    BRENDAi3.2.1.97. 11933.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH101. Glycoside Hydrolase Family 101.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-alpha-N-acetylgalactosaminidase (EC:3.2.1.97)
    Alternative name(s):
    SpGH101
    Gene namesi
    Ordered Locus Names:spr0328
    OrganismiStreptococcus pneumoniae (strain ATCC BAA-255 / R6)
    Taxonomic identifieri171101 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    Proteomesi
    • UP000000586 Componenti: Chromosome

    Subcellular locationi

    • Secretedcell wall PROSITE-ProRule annotation; Peptidoglycan-anchor PROSITE-ProRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell wall, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi658D → A: Large decrease in substrate affinity. 1 Publication1
    Mutagenesisi764D → A: Loss of activity. 1 Publication1
    Mutagenesisi796E → A or Q: Loss of activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 39Sequence analysisAdd BLAST39
    ChainiPRO_000040887040 – 1738Endo-alpha-N-acetylgalactosaminidaseAdd BLAST1699
    PropeptideiPRO_00004088711739 – 1767Removed by sortasePROSITE-ProRule annotationAdd BLAST29

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1738Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

    Keywords - PTMi

    Peptidoglycan-anchor

    Interactioni

    Protein-protein interaction databases

    STRINGi171101.spr0328.

    Structurei

    Secondary structure

    11767
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi124 – 127Combined sources4
    Helixi131 – 133Combined sources3
    Beta strandi136 – 142Combined sources7
    Beta strandi145 – 151Combined sources7
    Beta strandi158 – 161Combined sources4
    Beta strandi163 – 167Combined sources5
    Beta strandi178 – 186Combined sources9
    Beta strandi195 – 203Combined sources9
    Beta strandi206 – 213Combined sources8
    Beta strandi216 – 222Combined sources7
    Beta strandi243 – 250Combined sources8
    Beta strandi255 – 260Combined sources6
    Helixi273 – 279Combined sources7
    Beta strandi284 – 289Combined sources6
    Beta strandi298 – 302Combined sources5
    Beta strandi331 – 335Combined sources5
    Beta strandi337 – 348Combined sources12
    Beta strandi350 – 355Combined sources6
    Beta strandi358 – 362Combined sources5
    Beta strandi370 – 372Combined sources3
    Beta strandi375 – 377Combined sources3
    Beta strandi380 – 387Combined sources8
    Beta strandi390 – 399Combined sources10
    Helixi400 – 402Combined sources3
    Beta strandi404 – 415Combined sources12
    Beta strandi418 – 430Combined sources13
    Helixi441 – 443Combined sources3
    Beta strandi447 – 449Combined sources3
    Beta strandi455 – 459Combined sources5
    Beta strandi466 – 470Combined sources5
    Beta strandi481 – 485Combined sources5
    Beta strandi494 – 503Combined sources10
    Beta strandi508 – 513Combined sources6
    Beta strandi519 – 521Combined sources3
    Helixi522 – 524Combined sources3
    Beta strandi529 – 537Combined sources9
    Beta strandi539 – 546Combined sources8
    Helixi562 – 564Combined sources3
    Beta strandi569 – 576Combined sources8
    Beta strandi578 – 582Combined sources5
    Helixi586 – 593Combined sources8
    Turni594 – 596Combined sources3
    Helixi603 – 608Combined sources6
    Beta strandi609 – 616Combined sources8
    Helixi626 – 640Combined sources15
    Beta strandi644 – 650Combined sources7
    Helixi669 – 671Combined sources3
    Helixi673 – 685Combined sources13
    Turni686 – 688Combined sources3
    Beta strandi689 – 700Combined sources12
    Beta strandi704 – 706Combined sources3
    Turni709 – 711Combined sources3
    Beta strandi722 – 733Combined sources12
    Helixi735 – 740Combined sources6
    Helixi743 – 754Combined sources12
    Beta strandi760 – 765Combined sources6
    Helixi776 – 787Combined sources12
    Turni788 – 790Combined sources3
    Beta strandi792 – 796Combined sources5
    Beta strandi798 – 800Combined sources3
    Turni802 – 804Combined sources3
    Beta strandi806 – 808Combined sources3
    Helixi809 – 812Combined sources4
    Beta strandi814 – 817Combined sources4
    Beta strandi821 – 823Combined sources3
    Helixi827 – 833Combined sources7
    Turni834 – 836Combined sources3
    Helixi845 – 847Combined sources3
    Helixi849 – 851Combined sources3
    Beta strandi864 – 866Combined sources3
    Helixi867 – 869Combined sources3
    Helixi874 – 890Combined sources17
    Beta strandi893 – 900Combined sources8
    Beta strandi904 – 908Combined sources5
    Beta strandi911 – 915Combined sources5
    Beta strandi918 – 924Combined sources7
    Beta strandi930 – 936Combined sources7
    Helixi943 – 946Combined sources4
    Beta strandi948 – 952Combined sources5
    Beta strandi955 – 959Combined sources5
    Beta strandi962 – 967Combined sources6
    Helixi978 – 980Combined sources3
    Beta strandi982 – 989Combined sources8
    Beta strandi991 – 996Combined sources6
    Helixi999 – 1002Combined sources4
    Beta strandi1007 – 1012Combined sources6
    Beta strandi1015 – 1021Combined sources7
    Beta strandi1026 – 1032Combined sources7
    Beta strandi1039 – 1044Combined sources6
    Turni1053 – 1058Combined sources6
    Beta strandi1072 – 1076Combined sources5
    Helixi1078 – 1080Combined sources3
    Beta strandi1081 – 1085Combined sources5
    Beta strandi1091 – 1095Combined sources5
    Beta strandi1097 – 1100Combined sources4
    Beta strandi1102 – 1107Combined sources6
    Beta strandi1116 – 1125Combined sources10
    Beta strandi1127 – 1129Combined sources3
    Beta strandi1131 – 1136Combined sources6
    Beta strandi1141 – 1148Combined sources8
    Helixi1164 – 1166Combined sources3
    Beta strandi1176 – 1183Combined sources8
    Beta strandi1192 – 1197Combined sources6
    Beta strandi1199 – 1202Combined sources4
    Beta strandi1204 – 1213Combined sources10
    Beta strandi1219 – 1221Combined sources3
    Beta strandi1223 – 1225Combined sources3
    Beta strandi1230 – 1232Combined sources3
    Turni1240 – 1243Combined sources4
    Beta strandi1244 – 1246Combined sources3
    Beta strandi1251 – 1254Combined sources4
    Beta strandi1256 – 1261Combined sources6
    Turni1264 – 1267Combined sources4
    Helixi1271 – 1273Combined sources3
    Beta strandi1284 – 1290Combined sources7
    Beta strandi1296 – 1301Combined sources6
    Turni1303 – 1305Combined sources3
    Beta strandi1313 – 1324Combined sources12
    Beta strandi1327 – 1336Combined sources10
    Beta strandi1339 – 1341Combined sources3
    Helixi1346 – 1348Combined sources3
    Beta strandi1349 – 1353Combined sources5
    Beta strandi1365 – 1372Combined sources8
    Beta strandi1379 – 1385Combined sources7
    Helixi1397 – 1403Combined sources7
    Turni1404 – 1406Combined sources3
    Beta strandi1407 – 1418Combined sources12
    Helixi1422 – 1437Combined sources16
    Helixi1444 – 1450Combined sources7
    Helixi1452 – 1458Combined sources7
    Helixi1466 – 1475Combined sources10
    Helixi1477 – 1480Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ECQX-ray2.90A/B40-1567[»]
    ProteinModelPortaliQ8DR60.
    SMRiQ8DR60.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8DR60.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni602 – 893CatalyticAdd BLAST292

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi1735 – 1739LPXTG sorting signalPROSITE-ProRule annotation5

    Domaini

    Is a multimodular protein that comprises seven distinct domains. The catalytic glycoside hydrolase domain resides in domain 3 (residues 602-893). Possesses four potential carbohydrate-binding modules (CBMs).1 Publication

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiENOG4105ESP. Bacteria.
    ENOG410XRFZ. LUCA.
    HOGENOMiHOG000285069.
    KOiK17624.
    OMAiWHTSWNG.

    Family and domain databases

    CDDicd14244. GH_101_like. 1 hit.
    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR025706. Endoa_GalNAc.
    IPR000421. FA58C.
    IPR008979. Galactose-bd-like.
    IPR005877. YSIRK_signal_dom.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF12905. Glyco_hydro_101. 1 hit.
    PF04650. YSIRK_signal. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
    PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8DR60-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNKGLFEKRC KYSIRKFSLG VASVMIGATF FGTSPVLADS VQSGSTANLP
    60 70 80 90 100
    ADLATALATA KENDGHDFEA PKVGEDQGSP EVTDGPKTEE ELLALEKEKP
    110 120 130 140 150
    AEEKPKEDKP AAAKPETPKT VTPEWQTVEK KEQQGTVTIR EEKGVRYNQL
    160 170 180 190 200
    SSTAQNDNAG KPALFEKKGL TVDANGNATV DLTFKDDSEK GKSRFGVFLK
    210 220 230 240 250
    FKDTKNNVFV GYDKDGWFWE YKSPTTSTWY RGSRVAAPET GSTNRLSITL
    260 270 280 290 300
    KSDGQLNASN NDVNLFDTVT LPAAVNDHLK NEKKILLKAG SYDDERTVVS
    310 320 330 340 350
    VKTDNQEGVK TEDTPAEKET GPEVDDSKVT YDTIQSKVLK AVIDQAFPRV
    360 370 380 390 400
    KEYSLNGHTL PGQVQQFNQV FINNHRITPE VTYKKINETT AEYLMKLRDD
    410 420 430 440 450
    AHLINAEMTV RLQVVDNQLH FDVTKIVNHN QVTPGQKIDD ERKLLSSISF
    460 470 480 490 500
    LGNALVSVSS DQTGAKFDGA TMSNNTHVSG DDHIDVTNPM KDLAKGYMYG
    510 520 530 540 550
    FVSTDKLAAG VWSNSQNSYG GGSNDWTRLT AYKETVGNAN YVGIHSSEWQ
    560 570 580 590 600
    WEKAYKGIVF PEYTKELPSA KVVITEDANA DKKVDWQDGA IAYRSIMNNP
    610 620 630 640 650
    QGWKKVKDIT AYRIAMNFGS QAQNPFLMTL DGIKKINLHT DGLGQGVLLK
    660 670 680 690 700
    GYGSEGHDSG HLNYADIGKR IGGVEDFKTL IEKAKKYGAH LGIHVNASET
    710 720 730 740 750
    YPESKYFNEK ILRKNPDGSY SYGWNWLDQG INIDAAYDLA HGRLARWEDL
    760 770 780 790 800
    KKKLGDGLDF IYVDVWGNGQ SGDNGAWATH VLAKEINKQG WRFAIEWGHG
    810 820 830 840 850
    GEYDSTFHHW AADLTYGGYT NKGINSAITR FIRNHQKDAW VGDYRSYGGA
    860 870 880 890 900
    ANYPLLGGYS MKDFEGWQGR SDYNGYVTNL FAHDVMTKYF QHFTVSKWEN
    910 920 930 940 950
    GTPVTMTDNG STYKWTPEMR VELVDADNNK VVVTRKSNDV NSPQYRERTV
    960 970 980 990 1000
    TLNGRVIQDG SAYLTPWNWD ANGKKLSTDK EKMYYFNTQA GATTWTLPSD
    1010 1020 1030 1040 1050
    WAKSKVYLYK LTDQGKTEEQ ELTVKDGKIT LDLLANQPYV LYRSKQTNPE
    1060 1070 1080 1090 1100
    MSWSEGMHIY DQGFNSGTLK HWTISGDASK AEIVKSQGAN DMLRIQGNKE
    1110 1120 1130 1140 1150
    KVSLTQKLTG LKPNTKYAVY VGVDNRSNAK ASITVNTGEK EVTTYTNKSL
    1160 1170 1180 1190 1200
    ALNYVKAYAH NTRRNNATVD DTSYFQNMYA FFTTGSDVSN VTLTLSREAG
    1210 1220 1230 1240 1250
    DEATYFDEIR TFENNSSMYG DKHDTGKGTF KQDFENVAQG IFPFVVGGVE
    1260 1270 1280 1290 1300
    GVEDNRTHLS EKHDPYTQRG WNGKKVDDVI EGNWSLKTNG LVSRRNLVYQ
    1310 1320 1330 1340 1350
    TIPQNFRFEA GKTYRVTFEY EAGSDNTYAF VVGKGEFQSG RRGTQASNLE
    1360 1370 1380 1390 1400
    MHELPNTWTD SKKAKKATFL VTGAETGDTW VGIYSTGNAS NTRGDSGGNA
    1410 1420 1430 1440 1450
    NFRGYNDFMM DNLQIEEITL TGKMLTENAL KNYLPTVAMT NYTKESMDAL
    1460 1470 1480 1490 1500
    KEAVFNLSQA DDDISVEEAR AEIAKIEALK NALVQKKTAL VADDFASLTA
    1510 1520 1530 1540 1550
    PAQAQEGLAN AFDGNLSSLW HTSWGGGDVG KPATMVLKEA TEITGLRYVP
    1560 1570 1580 1590 1600
    RGSGSNGNLR DVKLVVTDES GKEHTFTATD WPDNNKPKDI DFGKTIKAKK
    1610 1620 1630 1640 1650
    IVLTGTKTYG DGGDKYQSAA ELIFTRPQVA ETPLDLSGYE AALAKAQKLT
    1660 1670 1680 1690 1700
    DKDNQEEVAS VQASMKYATD NHLLTERMVE YFADYLNQLK DSATKPDAPT
    1710 1720 1730 1740 1750
    VEKPEFKLSS VASDQGKTPD YKQEIARPET PEQILPATGE SQFDTALFLA
    1760
    SVSLALSALF VVKTKKD
    Length:1,767
    Mass (Da):196,144
    Last modified:March 1, 2003 - v1
    Checksum:i34231975797B7587
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99132.1.
    PIRiH97912.
    RefSeqiNP_357922.1. NC_003098.1.
    WP_001032523.1. NC_003098.1.

    Genome annotation databases

    EnsemblBacteriaiAAK99132; AAK99132; spr0328.
    GeneIDi934804.
    KEGGispr:spr0328.
    PATRICi19700491. VBIStrPne107296_0367.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE007317 Genomic DNA. Translation: AAK99132.1.
    PIRiH97912.
    RefSeqiNP_357922.1. NC_003098.1.
    WP_001032523.1. NC_003098.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ECQX-ray2.90A/B40-1567[»]
    ProteinModelPortaliQ8DR60.
    SMRiQ8DR60.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi171101.spr0328.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH101. Glycoside Hydrolase Family 101.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK99132; AAK99132; spr0328.
    GeneIDi934804.
    KEGGispr:spr0328.
    PATRICi19700491. VBIStrPne107296_0367.

    Phylogenomic databases

    eggNOGiENOG4105ESP. Bacteria.
    ENOG410XRFZ. LUCA.
    HOGENOMiHOG000285069.
    KOiK17624.
    OMAiWHTSWNG.

    Enzyme and pathway databases

    BioCyciSPNE171101:GJC8-318-MONOMER.
    BRENDAi3.2.1.97. 11933.

    Miscellaneous databases

    EvolutionaryTraceiQ8DR60.

    Family and domain databases

    CDDicd14244. GH_101_like. 1 hit.
    Gene3Di2.60.120.260. 1 hit.
    InterProiIPR025706. Endoa_GalNAc.
    IPR000421. FA58C.
    IPR008979. Galactose-bd-like.
    IPR005877. YSIRK_signal_dom.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF12905. Glyco_hydro_101. 1 hit.
    PF04650. YSIRK_signal. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    TIGRFAMsiTIGR01168. YSIRK_signal. 1 hit.
    PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiGH101_STRR6
    AccessioniPrimary (citable) accession number: Q8DR60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: March 1, 2003
    Last modified: November 2, 2016
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The hydrolysis reaction catalyzed by SpGH101 proceeds with retention of the anomeric configuration.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.